Pancreatic hormone (PP) [1] is a peptide synthesized in pancreatic islets of
Langherhans, which acts as a regulator of pancreatic and gastrointestinal
functions. A number of other active peptides are homologous to pancreatic
hormone:
Neuropeptide Y (NPY) [2], one of the most abundant peptides in the
mammalian nervous system. NPY is implicated in the control of feeding and
the secretion of the gonadotrophin-releasing hormone.
Peptide YY (PYY) [3]. PPY is a gut peptide that inhibits exocrine
pancreatic secretion, has a vasoconstrictory action and inhibits jejunal
and colonic mobility.
Various NPY and PYY-like polypeptides from fish and amphibians [4,5].
Neuropeptide F (NPF) from invertebrates such as worms and snail [6].
Skin peptide Tyr-Tyr (SPYY) from the frog Phyllomedusa bicolor. SPYY shows
a large spectra of antibacterial and antifungal activity.
All these peptides are 36 to 39 amino acids long. Like most active peptides,
their C-terminal is amidated and they are synthesized as larger protein
precursors. The signature for these peptides is based on the last 17 C-terminal residues, where three positions are completely conserved. A profile
was also developed that spans the whole peptide.
Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue.
Curry W.J. Shaw C. Johnston C.F. Thim L. Buchanan K.D.
Source
Comp. Biochem. Physiol. 101C:269-274(1992).
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